alexa Salivary apyrase of Aedes aegypti: characterization and secretory fate.


Biochemistry & Physiology: Open Access

Author(s): Ribeiro JM, Sarkis JJ, Rossignol PA, Spielman A

Abstract Share this page

Abstract Salivary gland homogenates of female adult Aedes aegypti hydrolyzed ATP and ADP thereby defining an apyrase activity. Activity is divalent cation dependent with an optimum pH of 9.0. ATPase and ADPase activities could not be dissociated thus suggesting the presence of a true apyrase enzyme. Apyrase activity is low on the day of emergence but increases to 160 mU per pair of glands on the second day. The site at which mosquitoes probed into warm polyacrylamide gels retains apyrase activity, confirming the secretory fate of this activity.
This article was published in Comp Biochem Physiol B and referenced in Biochemistry & Physiology: Open Access

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

Relevant Topics

Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version